Research workbench
The 1.8 ångström structure of calmodulin RS20 peptide complex
Analyse The 1.8 ångström structure of calmodulin RS20 peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QS7
- Type
- protein
- Length
- 326 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin; RS20
- UniProt
- P19038
- Ligands
- CA, NH2
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 4 distinct chains · 65% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 145 | 63% helix, 4% strand | — |
| B | RS20 | protein | 19 | 84% helix, 0% strand | P19038 |
| C | Calmodulin | protein | 144 | 62% helix, 6% strand | — |
| D | RS20 | protein | 18 | 83% helix, 0% strand | P19038 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.55 | 0.79 | 34 | empty |
| 2 | 154 | 0.46 | 0.76 | 26 | empty |
| 3 | 87 | 0.34 | 0.74 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1454 Ų buried · 18 hydrogen bonds · protein-protein
- C–D · 1371 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 424 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 1QS7 · The 1.8 angstrom structure of calmodulin rs20 peptide complex · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P19038
- Elsewhere: RCSB PDB 1QS7 · PDBe 1QS7 · UniProt P19038
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